While it is critical for a protein's structure to be unique and stable, changes in this structure are imperative for binding and catalysis. It is now evident that many protein recognition processes incorporate conformational changes as a requisite event for function. In this manner, protein structure and dynamics are intimately linked with biological activity via both large and small scale conformational fluctuations. Research efforts in the Jennings, Opella, Taylor, Handel, and Komives laboratories in the Department of Chemistry and Biochemistry at UCSD are directed, in general towards understanding the dynamics of protein and peptide folding, molecular recognition and the conformational switches that correlate the regulation of function. A key element in each of our research programs is the use of high-resolution NMR methods for structure elucidation, probing protein/ligand recognition mechanisms, understanding folding reactions and characterizing native peptide/protein dynamics. A major impediment to research progress in each of our laboratories is the fact that access to departmental instruments is restricted by the high demand of spectrometer time. Currently, the typical waiting time on the departmental biomolecular NMR spectrometers is 2 1/2 - 3 months. We are requesting funds for the purchase of a modern console for our 500 MHz Varian Unity NMR spectrometer. With a new console, the spectrometer will be capable of the full range of multidimensional NMR experiments for studies of isotopically labeled peptides and proteins. The replacement of solely the console with a new console with full PFG capabilities and equipping the instrument with a triple-resonance triple axis gradient probe will significantly enhance research efforts in each of our laboratories and the Department by allowing implementation and development of modern pulse sequences as well as affording enhanced sensitivity for demanding applications such as analysis of marginally soluble proteins and peptides. [unreadable] [unreadable]